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Protein

Sulfotransferase 1C4

Gene

SULT1C4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. May be involved in the activation of carcinogenic hydroxylamines. Shows activity towards p-nitrophenol and N-hydroxy-2-acetylamino-fluorene (N-OH-2AAF).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei115 – 1151Proton acceptorBy similarity
Binding sitei137 – 1371PAPS1 Publication
Binding sitei145 – 1451PAPS1 Publication
Binding sitei200 – 2001PAPS1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi55 – 606PAPS1 Publication
Nucleotide bindingi234 – 2396PAPS1 Publication
Nucleotide bindingi262 – 2665PAPS1 Publication

GO - Molecular functioni

  • sulfotransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BRENDAi2.8.2.1. 2681.
ReactomeiR-HSA-156584. Cytosolic sulfonation of small molecules.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfotransferase 1C4 (EC:2.8.2.-)
Short name:
ST1C4
Alternative name(s):
Sulfotransferase 1C2
Short name:
SULT1C#2
Gene namesi
Name:SULT1C4
Synonyms:SULT1C2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:11457. SULT1C4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162405070.

Chemistry

ChEMBLiCHEMBL1743296.

Polymorphism and mutation databases

BioMutaiSULT1C4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Sulfotransferase 1C4PRO_0000085137Add
BLAST

Proteomic databases

MaxQBiO75897.
PaxDbiO75897.
PRIDEiO75897.

PTM databases

iPTMnetiO75897.
PhosphoSiteiO75897.

Expressioni

Tissue specificityi

Expressed at high levels in fetal lung and kidney and at low levels in fetal heart, adult kidney, ovary and spinal chord.

Gene expression databases

BgeeiO75897.
CleanExiHS_SULT1C2.
HS_SULT1C4.
GenevisibleiO75897. HS.

Organism-specific databases

HPAiHPA034530.

Interactioni

Protein-protein interaction databases

BioGridi118082. 4 interactions.
STRINGi9606.ENSP00000272452.

Structurei

Secondary structure

1
302
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 224Combined sources
Beta strandi25 – 284Combined sources
Helixi29 – 335Combined sources
Helixi35 – 395Combined sources
Beta strandi48 – 536Combined sources
Helixi58 – 6912Combined sources
Helixi74 – 774Combined sources
Helixi82 – 854Combined sources
Turni94 – 963Combined sources
Helixi99 – 1057Combined sources
Beta strandi111 – 1144Combined sources
Helixi118 – 1203Combined sources
Helixi124 – 1274Combined sources
Beta strandi131 – 1366Combined sources
Helixi139 – 15214Combined sources
Helixi162 – 1709Combined sources
Helixi179 – 18911Combined sources
Beta strandi192 – 1998Combined sources
Helixi200 – 2056Combined sources
Helixi207 – 21812Combined sources
Helixi224 – 23310Combined sources
Helixi236 – 2405Combined sources
Turni243 – 2453Combined sources
Turni252 – 2543Combined sources
Turni257 – 2593Combined sources
Helixi270 – 2734Combined sources
Helixi277 – 29014Combined sources
Helixi295 – 2995Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AD1X-ray2.00A7-302[»]
2GWHX-ray1.80A/B7-302[»]
ProteinModelPortaliO75897.
SMRiO75897. Positions 15-302.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75897.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni113 – 1153Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Phylogenomic databases

eggNOGiKOG1584. Eukaryota.
ENOG4111H56. LUCA.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiO75897.
KOiK01025.
OMAiFPFLEMK.
OrthoDBiEOG7V49ZK.
PhylomeDBiO75897.
TreeFamiTF321745.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75897-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALHDMEDFT FDGTKRLSVN YVKGILQPTD TCDIWDKIWN FQAKPDDLLI
60 70 80 90 100
STYPKAGTTW TQEIVELIQN EGDVEKSKRA PTHQRFPFLE MKIPSLGSGL
110 120 130 140 150
EQAHAMPSPR ILKTHLPFHL LPPSLLEKNC KIIYVARNPK DNMVSYYHFQ
160 170 180 190 200
RMNKALPAPG TWEEYFETFL AGKVCWGSWH EHVKGWWEAK DKHRILYLFY
210 220 230 240 250
EDMKKNPKHE IQKLAEFIGK KLDDKVLDKI VHYTSFDVMK QNPMANYSSI
260 270 280 290 300
PAEIMDHSIS PFMRKGAVGD WKKHFTVAQN ERFDEDYKKK MTDTRLTFHF

QF
Length:302
Mass (Da):35,520
Last modified:March 7, 2006 - v2
Checksum:i905E1820A6E222F3
GO
Isoform 2 (identifier: O75897-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     99-173: Missing.

Show »
Length:227
Mass (Da):26,841
Checksum:iA66BD789AE8FF92F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51D → E.2 Publications
Corresponds to variant rs1402467 [ dbSNP | Ensembl ].
VAR_025404
Natural varianti68 – 681I → M.1 Publication
Corresponds to variant rs41322445 [ dbSNP | Ensembl ].
VAR_061889

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei99 – 17375Missing in isoform 2. 2 PublicationsVSP_056255Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055584 mRNA. Translation: AAC95519.1.
AF186263 Genomic DNA. Translation: AAF72810.1.
AK297851 mRNA. Translation: BAG60183.1.
DQ987914 Genomic DNA. Translation: ABI75348.1.
AC068941 Genomic DNA. Translation: AAY14742.1.
CH471182 Genomic DNA. Translation: EAW53886.1.
BC125043 mRNA. Translation: AAI25044.1.
CCDSiCCDS2077.1. [O75897-1]
RefSeqiNP_006579.2. NM_006588.2. [O75897-1]
XP_005263976.1. XM_005263919.2. [O75897-2]
UniGeneiHs.312644.

Genome annotation databases

EnsembliENST00000272452; ENSP00000272452; ENSG00000198075. [O75897-1]
ENST00000409309; ENSP00000387225; ENSG00000198075. [O75897-2]
GeneIDi27233.
KEGGihsa:27233.
UCSCiuc002tea.2. human. [O75897-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055584 mRNA. Translation: AAC95519.1.
AF186263 Genomic DNA. Translation: AAF72810.1.
AK297851 mRNA. Translation: BAG60183.1.
DQ987914 Genomic DNA. Translation: ABI75348.1.
AC068941 Genomic DNA. Translation: AAY14742.1.
CH471182 Genomic DNA. Translation: EAW53886.1.
BC125043 mRNA. Translation: AAI25044.1.
CCDSiCCDS2077.1. [O75897-1]
RefSeqiNP_006579.2. NM_006588.2. [O75897-1]
XP_005263976.1. XM_005263919.2. [O75897-2]
UniGeneiHs.312644.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AD1X-ray2.00A7-302[»]
2GWHX-ray1.80A/B7-302[»]
ProteinModelPortaliO75897.
SMRiO75897. Positions 15-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118082. 4 interactions.
STRINGi9606.ENSP00000272452.

Chemistry

ChEMBLiCHEMBL1743296.

PTM databases

iPTMnetiO75897.
PhosphoSiteiO75897.

Polymorphism and mutation databases

BioMutaiSULT1C4.

Proteomic databases

MaxQBiO75897.
PaxDbiO75897.
PRIDEiO75897.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272452; ENSP00000272452; ENSG00000198075. [O75897-1]
ENST00000409309; ENSP00000387225; ENSG00000198075. [O75897-2]
GeneIDi27233.
KEGGihsa:27233.
UCSCiuc002tea.2. human. [O75897-1]

Organism-specific databases

CTDi27233.
GeneCardsiSULT1C4.
H-InvDBHIX0029964.
HGNCiHGNC:11457. SULT1C4.
HPAiHPA034530.
MIMi608357. gene.
neXtProtiNX_O75897.
PharmGKBiPA162405070.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1584. Eukaryota.
ENOG4111H56. LUCA.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiO75897.
KOiK01025.
OMAiFPFLEMK.
OrthoDBiEOG7V49ZK.
PhylomeDBiO75897.
TreeFamiTF321745.

Enzyme and pathway databases

BRENDAi2.8.2.1. 2681.
ReactomeiR-HSA-156584. Cytosolic sulfonation of small molecules.

Miscellaneous databases

EvolutionaryTraceiO75897.
GeneWikiiSULT1C4.
GenomeRNAii27233.
NextBioi50095.
PROiO75897.
SOURCEiSearch...

Gene expression databases

BgeeiO75897.
CleanExiHS_SULT1C2.
HS_SULT1C4.
GenevisibleiO75897. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene."
    Sakakibara Y., Yanagisawa K., Katafuchi J., Ringer D.P., Takami Y., Nakayama T., Suiko M., Liu M.-C.
    J. Biol. Chem. 273:33929-33935(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-5.
    Tissue: Fetal lung.
  2. "Human sulfotransferases SULT1C1 and SULT1C2: cDNA characterization, gene cloning, and chromosomal localization."
    Freimuth R.R., Raftogianis R.B., Wood T.C., Moon E., Kim U.-J., Xu J., Siciliano M.J., Weinshilboum R.M.
    Genomics 65:157-165(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Heart.
  4. NIEHS SNPs program
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-5 AND MET-68.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  8. Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 7-302 IN COMPLEX WITH PAPS, FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiST1C4_HUMAN
AccessioniPrimary (citable) accession number: O75897
Secondary accession number(s): Q069I8, Q08AS5, Q53S63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: March 7, 2006
Last modified: May 11, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.